Reaction of cytochrome c in the electron-transport chain of Paracoccus denitrificans.
Reaction of cytochrome c in the electron-transport chain of Paracoccus denitrificans.
复制标题
脱氮副球菌电子传递链中细胞色素 c 的反应。
DOI：
10.1016/0005-2728(83)90196-2
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发表时间：
1983
期刊：
影响因子：
--
通讯作者：
Nava,ME
中科院分区：
文献类型：
--
作者：
Davies,HC;Smith,L;Nava,ME
The reaction of the cytochromecoxidase (ferrocytochromec:oxygen oxidoreductase, EC 1.9.3.1) ofParacoccus denitrificanscytoplasmic membranes with the endogenous cytochromecof the membranes was studied, as well as its interaction with added exogenous cytochromecfromP. denitrificansor bovine heart. The polarographic method was employed, usingN,N,N′,N′-tetramethyl-p-phenylenediamine plus ascorbate to reduce the cytochromec. We found that overall electron transport can proceed maximally while the cytochromecremains membrane bound; NADH or succinoxidase activities were not inhibited by the addition of substances which bind theP. denitrificanscytochromecstrongly. In contrast to our observations with the spectrophotometric method (Smith, L., Davies, H.C. and Nava, M.E. (1976) Biochemistry 15, 5827–5831), in the polarographic assays the membrane-bound oxidase reacts with about equal rapidity with exogenous bovine andP. denitrificanscytochromesc. The reaction of the oxidase with the endogenous cytochromecproceeds at high rates and preferentially to that with exogenous cytochromec; the reaction with the latter, but not the former is inhibited by positively charged poly(l-lysine). The cytochromecand the oxidase appear to be very closely associated on the membrane.
